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Protein

Leishmanolysin

Gene

gp63

Organism
Leishmania major
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has an integral role during the infection of macrophages in the mammalian host.

Catalytic activityi

Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-|-Leu-Lys-Lys-.

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi264Zinc; catalytic1
Active sitei2651
Metal bindingi268Zinc; catalytic1
Metal bindingi334Zinc; catalytic1

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: InterPro
  • metallopeptidase activity Source: ParkinsonsUK-UCL

GO - Biological processi

  • catabolism by symbiont of host protein Source: ParkinsonsUK-UCL
  • cell adhesion Source: UniProtKB-KW
  • modulation by symbiont of host inflammatory response Source: ParkinsonsUK-UCL
  • positive regulation by symbiont of host cytokine secretion Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.36. 2950.

Protein family/group databases

MEROPSiM08.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Leishmanolysin (EC:3.4.24.36)
Alternative name(s):
Cell surface protease
Major surface glycoprotein
Major surface protease
Promastigote surface endopeptidase
Protein gp63
Gene namesi
Name:gp63
OrganismiLeishmania major
Taxonomic identifieri5664 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi254Y → D: No significant effect on protein expression levels or catalytic activity. 1 Publication1
Mutagenesisi264H → F or Y: No detectable overexpression of mutant protein and hence little catalytic activity. 1 Publication1
Mutagenesisi265E → D: No significant effect on protein expression levels but almost abolishes catalytic activity. 1 Publication1
Mutagenesisi268H → N or Y: No detectable overexpression of mutant protein and hence little catalytic activity. 1 Publication1
Mutagenesisi300N → Q: Increases electrophoretic mobility of the protein. 1 Publication1
Mutagenesisi407N → Q: Increases electrophoretic mobility of the protein. 1 Publication1
Mutagenesisi534N → Q: Increases electrophoretic mobility of the protein. 1 Publication1
Mutagenesisi577N → L: Causes extracellular release of the protein. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 39Sequence analysisAdd BLAST39
PropeptideiPRO_000002866740 – 100Activation peptide1 PublicationAdd BLAST61
ChainiPRO_0000028668101 – 577LeishmanolysinAdd BLAST477
PropeptideiPRO_0000028669578 – 602Removed in mature formAdd BLAST25

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi125 ↔ 1421 Publication
Disulfide bondi191 ↔ 2301 Publication
Glycosylationi300N-linked (GlcNAc...)2 Publications1
Disulfide bondi314 ↔ 3861 Publication
Disulfide bondi393 ↔ 4551 Publication
Disulfide bondi406 ↔ 4251 Publication
Glycosylationi407N-linked (GlcNAc...)2 Publications1
Disulfide bondi415 ↔ 4891 Publication
Disulfide bondi466 ↔ 5101 Publication
Disulfide bondi515 ↔ 5651 Publication
Glycosylationi534N-linked (GlcNAc...)1 Publication1
Disulfide bondi535 ↔ 5581 Publication
Lipidationi577GPI-anchor amidated asparagine1 Publication1

Post-translational modificationi

The phosphatidylinositol moiety of the GPI-anchor contains a fully saturated, unbranched 1-O-alkyl chain (mainly C24:0) and a mixture of fully saturated unbranched 2-O-acyl chains (C12:0, C14:0, C16:0, and C18:0).

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Zymogen

PTM databases

UniCarbKBiP08148.

Miscellaneous databases

PMAP-CutDBP08148.

Structurei

Secondary structure

1602
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi111 – 114Combined sources4
Helixi116 – 119Combined sources4
Beta strandi131 – 133Combined sources3
Beta strandi135 – 137Combined sources3
Beta strandi139 – 141Combined sources3
Helixi144 – 146Combined sources3
Helixi150 – 158Combined sources9
Helixi160 – 169Combined sources10
Beta strandi172 – 174Combined sources3
Beta strandi177 – 181Combined sources5
Helixi191 – 193Combined sources3
Helixi198 – 202Combined sources5
Beta strandi205 – 207Combined sources3
Beta strandi209 – 215Combined sources7
Beta strandi226 – 232Combined sources7
Beta strandi238 – 244Combined sources7
Helixi247 – 249Combined sources3
Helixi256 – 269Combined sources14
Helixi274 – 279Combined sources6
Beta strandi283 – 287Combined sources5
Helixi289 – 291Combined sources3
Beta strandi296 – 299Combined sources4
Helixi302 – 312Combined sources11
Beta strandi320 – 322Combined sources3
Turni328 – 332Combined sources5
Beta strandi333 – 335Combined sources3
Turni337 – 339Combined sources3
Beta strandi346 – 348Combined sources3
Helixi356 – 364Combined sources9
Helixi372 – 374Combined sources3
Turni380 – 383Combined sources4
Helixi386 – 390Combined sources5
Beta strandi393 – 395Combined sources3
Beta strandi398 – 400Combined sources3
Turni402 – 404Combined sources3
Beta strandi420 – 425Combined sources6
Helixi435 – 437Combined sources3
Beta strandi440 – 442Combined sources3
Turni450 – 454Combined sources5
Beta strandi458 – 465Combined sources8
Helixi470 – 472Combined sources3
Turni475 – 477Combined sources3
Helixi478 – 480Combined sources3
Beta strandi487 – 494Combined sources8
Beta strandi506 – 516Combined sources11
Turni517 – 520Combined sources4
Beta strandi521 – 525Combined sources5
Beta strandi540 – 542Combined sources3
Helixi543 – 545Combined sources3
Beta strandi548 – 550Combined sources3
Beta strandi555 – 557Combined sources3
Helixi561 – 565Combined sources5
Helixi569 – 572Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LMLX-ray1.86A100-577[»]
ProteinModelPortaliP08148.
SMRiP08148.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08148.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M8 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2556. Eukaryota.
ENOG410XSAG. LUCA.

Family and domain databases

InterProiIPR001577. Peptidase_M8.
[Graphical view]
PANTHERiPTHR10942. PTHR10942. 1 hit.
PfamiPF01457. Peptidase_M8. 1 hit.
[Graphical view]
PRINTSiPR00782. LSHMANOLYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08148-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVDSSSTHR RRCVAARLVR LAAAGAAVTV AVGTAAAWAH AGALQHRCVH
60 70 80 90 100
DAMQARVRQS VADHHKAPGA VSAVGLPYVT LDAAHTAAAA DPRPGSARSV
110 120 130 140 150
VRDVNWGALR IAVSTEDLTD PAYHCARVGQ HVKDHAGAIV TCTAEDILTN
160 170 180 190 200
EKRDILVKHL IPQAVQLHTE RLKVQQVQGK WKVTDMVGDI CGDFKVPQAH
210 220 230 240 250
ITEGFSNTDF VMYVASVPSE EGVLAWATTC QTFSDGHPAV GVINIPAANI
260 270 280 290 300
ASRYDQLVTR VVTHEMAHAL GFSGPFFEDA RIVANVPNVR GKNFDVPVIN
310 320 330 340 350
SSTAVAKARE QYGCDTLEYL EVEDQGGAGS AGSHIKMRNA QDELMAPAAA
360 370 380 390 400
AGYYTALTMA IFQDLGFYQA DFSKAEVMPW GQNAGCAFLT NKCMEQSVTQ
410 420 430 440 450
WPAMFCNESE DAIRCPTSRL SLGACGVTRH PGLPPYWQYF TDPSLAGVSA
460 470 480 490 500
FMDYCPVVVP YSDGSCTQRA SEAHASLLPF NVFSDAARCI DGAFRPKATD
510 520 530 540 550
GIVKSYAGLC ANVQCDTATR TYSVQVHGSN DYTNCTPGLR VELSTVSNAF
560 570 580 590 600
EGGGYITCPP YVEVCQGNVQ AAKDGGNTAA GRRGPRAAAT ALLVAALLAV

AL
Length:602
Mass (Da):63,953
Last modified:April 1, 1990 - v2
Checksum:i982EF3245D87C43E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00647 Genomic DNA. Translation: CAA68673.1.
PIRiPL0221.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00647 Genomic DNA. Translation: CAA68673.1.
PIRiPL0221.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LMLX-ray1.86A100-577[»]
ProteinModelPortaliP08148.
SMRiP08148.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM08.001.

PTM databases

UniCarbKBiP08148.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG2556. Eukaryota.
ENOG410XSAG. LUCA.

Enzyme and pathway databases

BRENDAi3.4.24.36. 2950.

Miscellaneous databases

EvolutionaryTraceiP08148.
PMAP-CutDBP08148.

Family and domain databases

InterProiIPR001577. Peptidase_M8.
[Graphical view]
PANTHERiPTHR10942. PTHR10942. 1 hit.
PfamiPF01457. Peptidase_M8. 1 hit.
[Graphical view]
PRINTSiPR00782. LSHMANOLYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGP63_LEIMA
AccessioniPrimary (citable) accession number: P08148
Secondary accession number(s): P15906
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: April 1, 1990
Last modified: November 2, 2016
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.